Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells
Open accessAbstract
The matrix domain promotes plasma-membrane-specific binding of HIV-1 Gag through interaction with an acidic lipid phosphatidylinositol-(4,5)-bisphosphate. In in vitro systems, matrix-bound RNA suppresses Gag interactions with phosphatidylserine, an acidic lipid prevalent in various cytoplasmic membranes, thereby enhancing the lipid specificity of the matrix domain. Here we provide in vitro and cell-based evidence supporting the idea that this RNA-mediated suppression occurs in cells and hence is a physiologically relevant mechanism that prevents Gag from binding promiscuously to phosphatidylserine-containing membranes.
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In vitro liposome-binding assays initially reported that RNA binding to MA prevents Gag binding to non-PI(4,5)P2 membrane lipids.
“Using in vitro liposome-binding assays, it was initially reported that RNA binding to MA prevents Gag binding to non-PI(4,5)P 2 membrane lipids (78,79)”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [79]
Cites
Göttlinger, H. G., Sodroski, J. G., & Haseltine, W. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5781 · Cited by 841 · see citing works
Hill, C. P., Worthylake, D., Bancroft, D. P., Christensen, A. M., & Sundquist, W. I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.3099 · Cited by 473 · see citing works
Chan, R., Uchil, P. D., Jin, J., Shui, G., Ott, D. E., Mothes, W., & Wenk, M. R. (2008) · Journal of Virology · doi:10.1128/jvi.00981-08 · Cited by 282 · see citing works
Chukkapalli, V., Oh, S. J., & Ono, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908661107 · Cited by 229 · see citing works
Self-citationAnalysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids
Alfadhli, A., Still, A., & Barklis, E. (2009) · Journal of Virology · doi:10.1128/jvi.01197-09 · Cited by 145 · see citing works
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Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication
Jin, D., & Musier-Forsyth, K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002957 · Cited by 67 · see citing works
“Using in vitro liposome-binding assays, it was initially reported that RNA binding to MA prevents Gag binding to non-PI(4,5)P2 membrane lipids (78, 79) and that PI(4,5)P2 outcompetes RNA for MA interaction (80).”
Background
- Authors
- Chukkapalli, V., Inlora, J., Todd, G. C., & Ono, A.
- Affiliations
- University of Michigan (US)
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2013-06-15
- Volume
- 87
- Issue
- 12
- Pages
- 7155-7159
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC3676091
- OpenAlex
- W1997279728
- Cited by
- 76
- References
- 5
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 2 · 2021: 7 · 2020: 3 · 2019: 7 · 2018: 9 · 2017: 4 · 2016: 11 · 2015: 9 · 2014: 13 · 2013: 3
- FWCI
- 5.51
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Virology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM008353, T32GM145304)
- National Institute of Allergy and Infectious Diseases (R01AI071727)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- HIV-1 Gag, matrix domain, phosphatidylserine, phosphatidylinositol 4,5-bisphosphate, lipid specificity, membrane binding, viral assembly, plasma membrane
- MeSH terms
- Cell Membrane, HeLa Cells, Humans, Phosphatidylserines, Protein Binding, RNA, HIV-1, gag Gene Products, Human Immunodeficiency Virus
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